Birrer Sandbox 2: Difference between revisions

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Alcohol dehydrogenase (PDB id [[1htb]]), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen.


Alcohol dehydrogenase (ADH) is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The reaction is shown below: CH3CH2OH + NAD+ -> CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) <ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.<ref> The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.   
In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The reaction is shown below: CH3CH2OH + NAD+ -> CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) <ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.<ref> The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.   




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{{STRUCTURE_1htb |  PDB=1htb  |  SCENE=  }}
 




Revision as of 23:29, 1 March 2010

Alcohol Dehydrogenase

PDB ID 1htb

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1htb, resolution 2.40Å ()
Ligands: , , ,
Gene: HUMAN BETA3 CDNA (Homo sapiens)
Activity: Alcohol dehydrogenase, with EC number 1.1.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Alcohol dehydrogenase (PDB id 1htb), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen.

In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The reaction is shown below: CH3CH2OH + NAD+ -> CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) <ref>Voet, et. al. Fundamentals of Biochemistry: 3rd Edition. Hoboken: Wiley & Sons, Inc, 2008.<ref> The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.


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David Birrer
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